Understanding the Assembly of Macromolecular Structures

Many important molecules, like the ribosome (pictured), must be assembled from their component parts. Our lab uses computational and theoretical models to study the dynamics of such assembly processes

Most biological processes rely, in some form or another, on the action of large protein or protein-nucleic acid complexes. Protein synthesis, for example, is catalyzed by the ribosome, a massive molecular machine consisting of 3-4 large RNA molecules and 50-80 proteins, depending on the organism in question. Transcription, splicing, protein degradation and signaling all involve the action of similarly large complexes.

Cells do not synthesize these machines as fully formed entities, but rather as a set of components (e.g. individual proteins and nucleic acids) that must assemble into a higher-order structure in order to perform their functions. At its core, this assembly process is mediated by a set of intermolecular (binding) interactions. In our lab we use mathematical and computational modeling to examine how a set of interacting components assembles into a fully-formed macromolecular structure. We are actively considering the following areas:

Optimizing the assembly of ring-like structures

Understanding assembly in the context of large Protein-Protein Interaction networks

Developing methods to allow for the design of structures that will self-assemble efficiently

Our lab also has interests in modeling the dynamics of signaling networks and in analyzing and developing models of allometric scaling. Please see our research page for more information!